Compounds > podophyllotoxin
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podophyllotoxin and combretastatin a-4 disodium phosphate

podophyllotoxin has been researched along with combretastatin a-4 disodium phosphate in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's3 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chernyshova, NB; Ikizalp, NN; Kiselyov, AS; Kislyi, KA; Kuznetsov, SA; Lantow, M; Leitao, A; Lemcke, H; Oprea, T; Raihstat, MM; Samet, AV; Semenov, VV; Semenova, MN; Weiss, DG1
Bueno, O; Camarasa, MJ; Díaz, JF; Estévez-Gallego, J; Liekens, S; Noppen, S; Pérez-Pérez, MJ; Priego, EM; Quesada, E; Tobajas, G1
Bueno, O; Camarasa, MJ; Díaz, JF; Estévez-Gallego, J; Gargantilla, M; Liekens, S; Martins, S; Pérez-Pérez, MJ; Priego, EM1

Other Studies

3 other study(ies) available for podophyllotoxin and combretastatin a-4 disodium phosphate

ArticleYear
Novel derivatives of 1,3,4-oxadiazoles are potent mitostatic agents featuring strong microtubule depolymerizing activity in the sea urchin embryo and cell culture assays.
    European journal of medicinal chemistry, 2010, Volume: 45, Issue:5

    Topics: Animals; Antineoplastic Agents; Biological Assay; Cell Cycle; Cell Proliferation; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Humans; Microtubules; Mitosis; Models, Molecular; Molecular Structure; Oxadiazoles; Phenotype; Sea Urchins; Structure-Activity Relationship; Tumor Cells, Cultured

2010
Conformational mimetics of the α-methyl chalcone TUB091 binding tubulin: Design, synthesis and antiproliferative activity.
    European journal of medicinal chemistry, 2018, Mar-25, Volume: 148

    Topics: Animals; Antineoplastic Agents; Benzodioxoles; Binding Sites; Biomimetics; Cell Line; Cell Proliferation; Chalcones; Drug Design; Endothelial Cells; Humans; Neoplasms; Protein Conformation; Tubulin; Tubulin Modulators

2018
Diphenyl ether derivatives occupy the expanded binding site of cyclohexanedione compounds at the colchicine site in tubulin by movement of the αT5 loop.
    European journal of medicinal chemistry, 2019, Jun-01, Volume: 171

    Topics: Antineoplastic Agents; Binding Sites; Cell Cycle; Cell Line; Cell Proliferation; Colchicine; Crystallography, X-Ray; Cyclohexanones; Dose-Response Relationship, Drug; Drug Screening Assays, Antitumor; Humans; Models, Molecular; Molecular Structure; Phenyl Ethers; Structure-Activity Relationship; Tubulin

2019